Temperature dependence of intramolecular electron transfer as a probe for predenaturational changes in lysozyme.

Intramolecular electron transfer in hen egg-white lysozyme between tryptophan and tyrosine units was investigated by means of pulse radiolysis in the temperature range 288-333 K. An Arrhenius plot for the kinetics of this process shows a sharp break at approximately 303 K (30 degrees C) compatible with the trend noted earlier (cf P. Jolles, et al. BBA, 491, 354, (1977)) on the Arrhenius plot for kinetics of bacterial substrate digestion by lysozyme. The departure from linearity of the Arrhenius plot for intramolecular electron transfer is interpreted in terms of local intralobe fluctuations of the native structure of lysozyme. It is suggested that such an approach can be useful for probing predenaturational changes in proteins.